Human UDP-α-D-xylose synthase forms a catalytically important tetramer that has not been observed in crystal structures

Biochemistry

Volumn 52, Issue 22, 2013, Pages 3888-3898

  Polizzi, Samuel J ^a   Walsh, Richard M ^a   Le Magueres, Pierre ^b   Criswell, Angela R ^b   Wood, Zachary A ^a  

^a University of Georgia ^*  (United States)

^b RIGAKU CORPORATION   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

DIMERS; ENZYMES; REACTION INTERMEDIATES; SIMULATED ANNEALING;

CRYSTALLOGRAPHIC STUDIES; CRYSTALS STRUCTURES; D-XYLOSE; HIGH ACTIVITY; QUATERNARY STRUCTURE; REDUCTASE ENZYMES; SHORTER CHAINS; SMALL ANGLE X-RAY SCATTERING; SYNTHASES; TETRAMERS;

X RAY SCATTERING;

DIMER; TETRAMER; TRIMETHYLAMINE OXIDE; UNCLASSIFIED DRUG; URIDINE DIPHOSPHATE ALPHA DEXTRO XYLOSE SYNTHASE; URIDINE DIPHOSPHATE XYLOSE;

ARTICLE; CARBOHYDRATE SYNTHESIS; CATALYSIS; CHEMICAL STRUCTURE; CONTROLLED STUDY; CRYSTAL STRUCTURE; DISSOCIATION CONSTANT; ENZYME ACTIVITY; ISOTHERM; PRIORITY JOURNAL; SEDIMENTATION RATE; ULTRACENTRIFUGATION; X RAY CRYSTALLOGRAPHY;

EID: 84878629479     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi400294e     Document Type: Article

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